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Volumn 54, Issue 31, 2015, Pages 4805-4814

Hydrogen/Deuterium Exchange and Molecular Dynamics Analysis of Amyloid Fibrils Formed by a D69K Charge-Pair Mutant of Human Apolipoprotein C-II

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; ELECTRIC CHARGE; GLYCOPROTEINS; LIPOPROTEINS; OLIGOMERS; POLYPEPTIDES; X RAY DIFFRACTION;

EID: 84938680564     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b00535     Document Type: Article
Times cited : (13)

References (37)
  • 1
    • 0033849738 scopus 로고    scopus 로고
    • Review: History of the amyloid fibril
    • Sipe, J. D. and Cohen, A. S. (2000) Review: history of the amyloid fibril J. Struct. Biol. 130, 88-98 10.1006/jsbi.2000.4221
    • (2000) J. Struct. Biol. , vol.130 , pp. 88-98
    • Sipe, J.D.1    Cohen, A.S.2
  • 2
    • 0028866543 scopus 로고
    • Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques
    • Westermark, P., Mucchiano, G., Marthin, T., Johnson, K. H., and Sletten, K. (1995) Apolipoprotein A1-derived amyloid in human aortic atherosclerotic plaques Am. J. Pathol. 147, 1186-1192
    • (1995) Am. J. Pathol. , vol.147 , pp. 1186-1192
    • Westermark, P.1    Mucchiano, G.2    Marthin, T.3    Johnson, K.H.4    Sletten, K.5
  • 3
    • 0026052592 scopus 로고
    • Polymorphism of apolipoprotein A-II (apoA-II) among inbred strains of mice. Relationship between the molecular type of apoA-II and mouse senile amyloidosis
    • Higuchi, K., Kitagawa, K., Naiki, H., Hanada, K., Hosokawa, M., and Takeda, T. (1991) Polymorphism of apolipoprotein A-II (apoA-II) among inbred strains of mice. Relationship between the molecular type of apoA-II and mouse senile amyloidosis Biochem. J. 279 (Part 2) 427-433
    • (1991) Biochem. J. , vol.279 , Issue.PART 2 , pp. 427-433
    • Higuchi, K.1    Kitagawa, K.2    Naiki, H.3    Hanada, K.4    Hosokawa, M.5    Takeda, T.6
  • 4
    • 3543107213 scopus 로고    scopus 로고
    • Two different types of amyloid deposits - Apolipoprotein A-IV and transthyretin - In a patient with systemic amyloidosis
    • Bergstrom, J., Murphy, C. L., Weiss, D. T., Solomon, A., Sletten, K., Hellman, U., and Westermark, P. (2004) Two different types of amyloid deposits - apolipoprotein A-IV and transthyretin - in a patient with systemic amyloidosis Lab. Invest. 84, 981-988 10.1038/labinvest.3700124
    • (2004) Lab. Invest. , vol.84 , pp. 981-988
    • Bergstrom, J.1    Murphy, C.L.2    Weiss, D.T.3    Solomon, A.4    Sletten, K.5    Hellman, U.6    Westermark, P.7
  • 6
    • 0028924083 scopus 로고
    • Is Alzheimer's disease an apolipoprotein e amyloidosis?
    • Wisniewski, T., Lalowski, M., Golabek, A., Vogel, T., and Frangione, B. (1995) Is Alzheimer's disease an apolipoprotein E amyloidosis? Lancet 345, 956-958 10.1016/S0140-6736(95)90701-7
    • (1995) Lancet , vol.345 , pp. 956-958
    • Wisniewski, T.1    Lalowski, M.2    Golabek, A.3    Vogel, T.4    Frangione, B.5
  • 7
    • 0032508364 scopus 로고    scopus 로고
    • Comparison of apolipoprotein and proteoglycan deposits in human coronary atherosclerotic plaques: Colocalization of biglycan with apolipoproteins
    • O'Brien, K. D., Olin, K. L., Alpers, C. E., Chiu, W., Ferguson, M., Hudkins, K., Wight, T. N., and Chait, A. (1998) Comparison of apolipoprotein and proteoglycan deposits in human coronary atherosclerotic plaques: colocalization of biglycan with apolipoproteins Circulation 98, 519-527 10.1161/01.CIR.98.6.519
    • (1998) Circulation , vol.98 , pp. 519-527
    • O'Brien, K.D.1    Olin, K.L.2    Alpers, C.E.3    Chiu, W.4    Ferguson, M.5    Hudkins, K.6    Wight, T.N.7    Chait, A.8
  • 9
    • 79953215653 scopus 로고    scopus 로고
    • Apolipoproteins and amyloid fibril formation in atherosclerosis
    • Teoh, C. L., Griffin, M. D., and Howlett, G. J. (2011) Apolipoproteins and amyloid fibril formation in atherosclerosis Protein Cell 2, 116-127 10.1007/s13238-011-1013-6
    • (2011) Protein Cell , vol.2 , pp. 116-127
    • Teoh, C.L.1    Griffin, M.D.2    Howlett, G.J.3
  • 10
    • 0023943675 scopus 로고
    • The apolipoprotein multigene family: Biosynthesis, structure, structure-function relationships, and evolution
    • Li, W. H., Tanimura, M., Luo, C. C., Datta, S., and Chan, L. (1988) The apolipoprotein multigene family: biosynthesis, structure, structure-function relationships, and evolution J. Lipid Res. 29, 245-271
    • (1988) J. Lipid Res. , vol.29 , pp. 245-271
    • Li, W.H.1    Tanimura, M.2    Luo, C.C.3    Datta, S.4    Chan, L.5
  • 11
    • 0028216402 scopus 로고
    • The amphipathic alpha helix: A multifunctional structural motif in plasma apolipoproteins
    • Segrest, J. P., Garber, D. W., Brouillette, C. G., Harvey, S. C., and Anantharamaiah, G. M. (1994) The amphipathic alpha helix: a multifunctional structural motif in plasma apolipoproteins Adv. Protein Chem. 45, 303-369 10.1016/S0065-3233(08)60643-9
    • (1994) Adv. Protein Chem. , vol.45 , pp. 303-369
    • Segrest, J.P.1    Garber, D.W.2    Brouillette, C.G.3    Harvey, S.C.4    Anantharamaiah, G.M.5
  • 12
    • 0036520326 scopus 로고    scopus 로고
    • The structural basis for amyloid formation by plasma apolipoproteins: A review
    • Hatters, D. M. and Howlett, G. J. (2002) The structural basis for amyloid formation by plasma apolipoproteins: a review Eur. Biophys. J. 31, 2-8 10.1007/s002490100172
    • (2002) Eur. Biophys. J. , vol.31 , pp. 2-8
    • Hatters, D.M.1    Howlett, G.J.2
  • 14
    • 0033578448 scopus 로고    scopus 로고
    • Helix-helix association of a lipid-bound amphipathic alpha-helix derived from apolipoprotein C-II
    • MacPhee, C. E., Howlett, G. J., Sawyer, W. H., and Clayton, A. H. (1999) Helix-helix association of a lipid-bound amphipathic alpha-helix derived from apolipoprotein C-II Biochemistry 38, 10878-10884 10.1021/bi990726b
    • (1999) Biochemistry , vol.38 , pp. 10878-10884
    • MacPhee, C.E.1    Howlett, G.J.2    Sawyer, W.H.3    Clayton, A.H.4
  • 15
    • 4043102703 scopus 로고
    • Activation of lipoprotein lipase by native and synthetic fragments of human plasma apolipoprotein C-II
    • Kinnunen, P. K., Jackson, R. L., Smith, L. C., Gotto, A. M., Jr., and Sparrow, J. T. (1977) Activation of lipoprotein lipase by native and synthetic fragments of human plasma apolipoprotein C-II Proc. Natl. Acad. Sci. U. S. A. 74, 4848-4851 10.1073/pnas.74.11.4848
    • (1977) Proc. Natl. Acad. Sci. U. S. A. , vol.74 , pp. 4848-4851
    • Kinnunen, P.K.1    Jackson, R.L.2    Smith, L.C.3    Gotto, A.M.4    Sparrow, J.T.5
  • 16
    • 84923163748 scopus 로고    scopus 로고
    • Charge and Charge-Pair Mutations Alter the Rate of Assembly and Structural Properties of Apolipoprotein C-II Amyloid Fibrils
    • Mao, Y., Teoh, C. L., Yang, S., Zlatic, C. O., Rosenes, Z. K., Gooley, P. R., Howlett, G. J., and Griffin, M. D. (2015) Charge and Charge-Pair Mutations Alter the Rate of Assembly and Structural Properties of Apolipoprotein C-II Amyloid Fibrils Biochemistry 54, 1421-1428 10.1021/bi5014535
    • (2015) Biochemistry , vol.54 , pp. 1421-1428
    • Mao, Y.1    Teoh, C.L.2    Yang, S.3    Zlatic, C.O.4    Rosenes, Z.K.5    Gooley, P.R.6    Howlett, G.J.7    Griffin, M.D.8
  • 17
    • 0031627465 scopus 로고    scopus 로고
    • An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli
    • Cai, M., Huang, Y., Sakaguchi, K., Clore, G. M., Gronenborn, A. M., and Craigie, R. (1998) An efficient and cost-effective isotope labeling protocol for proteins expressed in Escherichia coli J. Biomol. NMR 11, 97-102 10.1023/A:1008222131470
    • (1998) J. Biomol. NMR , vol.11 , pp. 97-102
    • Cai, M.1    Huang, Y.2    Sakaguchi, K.3    Clore, G.M.4    Gronenborn, A.M.5    Craigie, R.6
  • 18
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley, J., Lu, M., and Bracken, C. (2001) A method for efficient isotopic labeling of recombinant proteins J. Biomol. NMR 20, 71-75 10.1023/A:1011254402785
    • (2001) J. Biomol. NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 19
    • 0036242430 scopus 로고    scopus 로고
    • Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange
    • Hoshino, M., Katou, H., Hagihara, Y., Hasegawa, K., Naiki, H., and Goto, Y. (2002) Mapping the core of the beta(2)-microglobulin amyloid fibril by H/D exchange Nat. Struct. Biol. 9, 332-336 10.1038/nsb792
    • (2002) Nat. Struct. Biol. , vol.9 , pp. 332-336
    • Hoshino, M.1    Katou, H.2    Hagihara, Y.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 20
    • 0028966761 scopus 로고
    • Rapid Amide Proton-Exchange Rates in Peptides and Proteins Measured by Solvent Quenching and 2-Dimensional Nmr
    • Zhang, Y. Z., Paterson, Y., and Roder, H. (1995) Rapid Amide Proton-Exchange Rates in Peptides and Proteins Measured by Solvent Quenching and 2-Dimensional Nmr Protein Sci. 4, 804-814 10.1002/pro.5560040420
    • (1995) Protein Sci. , vol.4 , pp. 804-814
    • Zhang, Y.Z.1    Paterson, Y.2    Roder, H.3
  • 21
    • 1842786897 scopus 로고    scopus 로고
    • Core and heterogeneity of beta(2)-microglobulin amyloid fibrils as revealed by H/D exchange
    • Yamaguchi, K. I., Katou, H., Hoshino, M., Hasegawa, K., Naiki, H., and Goto, Y. (2004) Core and heterogeneity of beta(2)-microglobulin amyloid fibrils as revealed by H/D exchange J. Mol. Biol. 338, 559-571 10.1016/j.jmb.2004.02.067
    • (2004) J. Mol. Biol. , vol.338 , pp. 559-571
    • Yamaguchi, K.I.1    Katou, H.2    Hoshino, M.3    Hasegawa, K.4    Naiki, H.5    Goto, Y.6
  • 22
    • 0029400480 scopus 로고
    • NMRPipe: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPipe: a multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293 10.1007/BF00197809
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 23
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson, B. A. and Blevins, R. A. (1994) NMR View: A computer program for the visualization and analysis of NMR data J. Biomol. NMR 4, 603-614 10.1007/BF00404272
    • (1994) J. Biomol. NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 24
    • 0032879438 scopus 로고    scopus 로고
    • X-ray fiber diffraction of amyloid fibrils
    • Serpell, L. C., Fraser, P. E., and Sunde, M. (1999) X-ray fiber diffraction of amyloid fibrils Methods Enzymol. 309, 526-536 10.1016/S0076-6879(99)09036-9
    • (1999) Methods Enzymol. , vol.309 , pp. 526-536
    • Serpell, L.C.1    Fraser, P.E.2    Sunde, M.3
  • 25
    • 34548599694 scopus 로고    scopus 로고
    • CLEARER: A new tool for the analysis of X-ray fibre diffraction patterns and diffraction simulation from atomic structural models
    • Sumner Makin, O., Sikorski, P., and Serpell, L. C. (2007) CLEARER: a new tool for the analysis of X-ray fibre diffraction patterns and diffraction simulation from atomic structural models J. Appl. Crystallogr. 40, 966-972 10.1107/S0021889807034681
    • (2007) J. Appl. Crystallogr. , vol.40 , pp. 966-972
    • Sumner Makin, O.1    Sikorski, P.2    Serpell, L.C.3
  • 26
    • 33846086933 scopus 로고    scopus 로고
    • Canonical sampling through velocity rescaling
    • Bussi, G., Donadio, D., and Parrinello, M. (2007) Canonical sampling through velocity rescaling J. Chem. Phys. 126, 014101 10.1063/1.2408420
    • (2007) J. Chem. Phys. , vol.126 , pp. 014101
    • Bussi, G.1    Donadio, D.2    Parrinello, M.3
  • 27
    • 0019707626 scopus 로고
    • Polymorphic Transitions in Single-Crystals - A New Molecular-Dynamics Method
    • Parrinello, M. and Rahman, A. (1981) Polymorphic Transitions in Single-Crystals-a New Molecular-Dynamics Method J. Appl. Phys. 52, 7182-7190 10.1063/1.328693
    • (1981) J. Appl. Phys. , vol.52 , pp. 7182-7190
    • Parrinello, M.1    Rahman, A.2
  • 28
    • 0000388705 scopus 로고    scopus 로고
    • LINCS: A linear constraint solver for molecular simulations
    • Hess, B., Bekker, H., Berendsen, H. J. C., and Fraaije, J. G. E. M. (1997) LINCS: A linear constraint solver for molecular simulations J. Comput. Chem. 18, 1463-1472 10.1002/(SICI)1096-987X(199709)18:12<1463::AID-JCC4>3.3.CO;2-L
    • (1997) J. Comput. Chem. , vol.18 , pp. 1463-1472
    • Hess, B.1    Bekker, H.2    Berendsen, H.J.C.3    Fraaije, J.G.E.M.4
  • 29
    • 0029878720 scopus 로고    scopus 로고
    • VMD: Visual molecular dynamics
    • Humphrey, W., Dalke, A., and Schulten, K. (1996) VMD: Visual molecular dynamics J. Mol. Graphics 14, 33-38 10.1016/0263-7855(96)00018-5
    • (1996) J. Mol. Graphics , vol.14 , pp. 33-38
    • Humphrey, W.1    Dalke, A.2    Schulten, K.3
  • 31
    • 33846847762 scopus 로고    scopus 로고
    • A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis
    • Wilson, L. M., Mok, Y. F., Binger, K. J., Griffin, M. D., Mertens, H. D., Lin, F., Wade, J. D., Gooley, P. R., and Howlett, G. J. (2007) A structural core within apolipoprotein C-II amyloid fibrils identified using hydrogen exchange and proteolysis J. Mol. Biol. 366, 1639-1651 10.1016/j.jmb.2006.12.040
    • (2007) J. Mol. Biol. , vol.366 , pp. 1639-1651
    • Wilson, L.M.1    Mok, Y.F.2    Binger, K.J.3    Griffin, M.D.4    Mertens, H.D.5    Lin, F.6    Wade, J.D.7    Gooley, P.R.8    Howlett, G.J.9
  • 32
    • 0031592945 scopus 로고    scopus 로고
    • Common core structure of amyloid fibrils by synchrotron X-ray diffraction
    • Sunde, M., Serpell, L. C., Bartlam, M., Fraser, P. E., Pepys, M. B., and Blake, C. C. (1997) Common core structure of amyloid fibrils by synchrotron X-ray diffraction J. Mol. Biol. 273, 729-739 10.1006/jmbi.1997.1348
    • (1997) J. Mol. Biol. , vol.273 , pp. 729-739
    • Sunde, M.1    Serpell, L.C.2    Bartlam, M.3    Fraser, P.E.4    Pepys, M.B.5    Blake, C.C.6
  • 34
    • 44349125669 scopus 로고    scopus 로고
    • Direct evidence for deprotonation of a lysine side chain buried in the hydrophobic core of a protein
    • Takayama, Y., Castaneda, C. A., Chimenti, M., Garcia-Moreno, B., and Iwahara, J. (2008) Direct evidence for deprotonation of a lysine side chain buried in the hydrophobic core of a protein J. Am. Chem. Soc. 130, 6714-6715 10.1021/ja801731g
    • (2008) J. Am. Chem. Soc. , vol.130 , pp. 6714-6715
    • Takayama, Y.1    Castaneda, C.A.2    Chimenti, M.3    Garcia-Moreno, B.4    Iwahara, J.5
  • 36
    • 84897063460 scopus 로고    scopus 로고
    • Local interactions influence the fibrillation kinetics, structure and dynamics of A beta(1-40) but leave the general fibril structure unchanged
    • Adler, J., Scheidt, H. A., Kruger, M., Thomas, L., and Huster, D. (2014) Local interactions influence the fibrillation kinetics, structure and dynamics of A beta(1-40) but leave the general fibril structure unchanged Phys. Chem. Chem. Phys. 16, 7461-7471 10.1039/c3cp54501f
    • (2014) Phys. Chem. Chem. Phys. , vol.16 , pp. 7461-7471
    • Adler, J.1    Scheidt, H.A.2    Kruger, M.3    Thomas, L.4    Huster, D.5
  • 37
    • 84901992350 scopus 로고    scopus 로고
    • 3D Hydrophobic Moment Vectors as a Tool to Characterize the Surface Polarity of Amphiphilic Peptides
    • Reisser, S., Strandberg, E., Steinbrecher, T., and Ulrich, A. S. (2014) 3D Hydrophobic Moment Vectors as a Tool to Characterize the Surface Polarity of Amphiphilic Peptides Biophys. J. 106, 2385-2394 10.1016/j.bpj.2014.04.020
    • (2014) Biophys. J. , vol.106 , pp. 2385-2394
    • Reisser, S.1    Strandberg, E.2    Steinbrecher, T.3    Ulrich, A.S.4


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